SCXC_ANDAU
ID SCXC_ANDAU Reviewed; 72 AA.
AC Q9BLM0;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Probable neurotoxin pcD-993;
DE Flags: Precursor;
OS Androctonus australis (Sahara scorpion).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC Scorpiones; Buthida; Buthoidea; Buthidae; Androctonus.
OX NCBI_TaxID=6858;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hector;
RX PubMed=11311249; DOI=10.1016/s0014-5793(01)02336-5;
RA Ceard B., Martin-Eauclaire M.-F., Bougis P.E.;
RT "Evidence for a position-specific deletion as an evolutionary link between
RT long- and short-chain scorpion toxins.";
RL FEBS Lett. 494:246-248(2001).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the long (3 C-C) scorpion toxin superfamily.
CC {ECO:0000305}.
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DR EMBL; AJ308444; CAC37325.1; -; mRNA.
DR AlphaFoldDB; Q9BLM0; -.
DR SMR; Q9BLM0; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019871; F:sodium channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR Gene3D; 3.30.30.10; -; 1.
DR InterPro; IPR044062; LCN-type_CS_alpha_beta_dom.
DR InterPro; IPR003614; Scorpion_toxin-like.
DR InterPro; IPR036574; Scorpion_toxin-like_sf.
DR InterPro; IPR002061; Scorpion_toxinL/defensin.
DR Pfam; PF00537; Toxin_3; 1.
DR SMART; SM00505; Knot1; 1.
DR SUPFAM; SSF57095; SSF57095; 1.
DR PROSITE; PS51863; LCN_CSAB; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Ion channel impairing toxin; Neurotoxin; Secreted; Signal;
KW Toxin.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..71
FT /note="Probable neurotoxin pcD-993"
FT /id="PRO_0000035227"
FT PROPEP 72
FT /note="Removed by a carboxypeptidase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000035228"
FT DOMAIN 21..72
FT /note="LCN-type CS-alpha/beta"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 35..56
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 42..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
FT DISULFID 46..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01210"
SQ SEQUENCE 72 AA; 7795 MW; 02F6CF9DF46C5D24 CRC64;
MNYLVMISFA LLLVIGVESV RDGYFVEPDN CVVHCMPSSE MCDRGCKHNG ATSGSCKAFS
KGGNACWCKG LR